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Literature summary extracted from

  • Kulik, V.; Hartmann, E.; Weyand, M.; Frey, M.; Gierl, A.; Niks, D.; Dunn, M.F.; Schlichting, I.
    On the structural basis of the catalytic mechanism and the regulation of the alpha subunit of tryptophan synthase from Salmonella typhimurium and BX1 from maize, two evolutionarily related enzymes (2005), J. Mol. Biol., 352, 608-620.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.8 expressed in Escherichia coli Zea mays

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.2.8 the crystal structure of BX1 suggusts that the faster catalytic rate of BX1 compared to the homologous alpha-subuni8t of tryptophan synthase EC 4.2.1.20, may due to a stabilzation of the active conformation, loop alphaL6 is closed and the catalytic glutamate, Glu134 is in the active conformation. There are two crystallographically independent molecules in the asymmetric unit of the rhombohedral BX1 crystal form Zea mays
4.2.1.20 crystal structures of the alpha-subunit of tryptophan synthase alone and in the alpha2beta2 complex Salmonella enterica subsp. enterica serovar Typhimurium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.2.8 plastid
-
 Zea mays 9536
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.2.8 indole-3-glycerol phosphate Zea mays the indole is further converted to 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, a secondary plant metabolite. BX1 cleaves indole-3-glycerol phosphate significantly faster to indole and glyceraldehyde 3-phosphate than the homologous alpha-subunit of tryptophan synthase, EC 4.2.1.20 indole + glyceraldehyde 3-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.8 Zea mays P42390
-
-
4.2.1.20 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.8
-
 Zea mays

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.2.8 (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate the indole is further converted to 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, a secondary plant metabolite. BX1 cleaves indole-3-glycerol phosphate significantly faster to indole and glyceraldehyde 3-phosphate than the homologous alpha-subunit of tryptophan synthase, EC 4.2.1.20. In the primary metabolism, indole diffuses through the connecting tunnel to the beta-active site where it is condensed with serine to form tryptophan and water Zea mays
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.1.2.8 seedling
-
 Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.8 indole-3-glycerol phosphate
-
 Zea mays indole + glyceraldehyde 3-phosphate
-
 ?
4.1.2.8 indole-3-glycerol phosphate the indole is further converted to 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, a secondary plant metabolite. BX1 cleaves indole-3-glycerol phosphate significantly faster to indole and glyceraldehyde 3-phosphate than the homologous alpha-subunit of tryptophan synthase, EC 4.2.1.20 Zea mays indole + glyceraldehyde 3-phosphate
-
 ?
4.2.1.20 indole-3-glycerol phosphate reaction is catalyzed by alpha-subunit. Structural basis of the catalytic mechanism and regulation of the alpha-subunit Salmonella enterica subsp. enterica serovar Typhimurium indole + D-glyceraldehyde 3-phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.2.8 BX1 a homolog of the alpha-subunit of bifunctional trypthophan synthase Zea mays
4.2.1.20 TRPS
-
 Salmonella enterica subsp. enterica serovar Typhimurium